The influence of sodium phosphate buffer on the stability of various proteins: Insights into protein-buffer interactions

2021 ◽  
pp. 115753
Author(s):  
Pannuru Pavani ◽  
Krishan Kumar ◽  
Anjeeta Rani ◽  
Pannuru Venkatesu ◽  
Ming-Jer Lee
Keyword(s):  
Phosphate Buffer ◽  
Sodium Phosphate ◽  
Sodium Phosphate Buffer ◽  
The Stability

Effects of sodium phosphate buffer on horseradish peroxidase thermal stability

2008 ◽  
Vol 93 (2) ◽  
pp. 569-574 ◽  
Author(s):  
L. Haifeng ◽  
L. Yuwen ◽  
C. Xiaomin ◽  
W. Zhiyong ◽  
W. Cunxin
Keyword(s):  
Thermal Stability ◽  
Horseradish Peroxidase ◽  
Phosphate Buffer ◽  
Sodium Phosphate ◽  
Sodium Phosphate Buffer

Recovery of milk fat globule membrane (MFGM) from buttermilk: effect of Ca-binding salts

2019 ◽  
Vol 86 (3) ◽  
pp. 374-376 ◽  
Author(s):  
Vitaly L. Spitsberg ◽  
Liza Ivanov ◽  
Vladimir Shritz
Keyword(s):  
Phosphate Buffer ◽  
Milk Fat ◽  
Sodium Phosphate ◽  
Milk Fat Globule Membrane ◽  
Peripheral Protein ◽  
Sodium Phosphate Buffer ◽  
Milk Fat Globule ◽  
Fat Globule ◽  
First Time ◽  
Phosphate Groups

AbstractIn this Research Communication we present a study of the effect of Ca-binding salts on the recovery of milk fat globule membrane (MFGM) from buttermilk. Sodium phosphate buffer was used for the purpose of MFGM recovery from buttermilk for the first time and we showed that 0.1 M buffer at pH 7.2 was the most effective for the recovery of MFGM. The fact of high efficacy of sodium phosphate buffer in recovery of MFGM from buttermilk allowed us to suggest that MFGM in buttermilk is present in association with casein through Ca- bridges formed between phospholipids of MFGM and phosphate groups of casein, primarily with k-casein as the peripheral protein of casein micelles.

scholarly journals Large-scale purification of hepatitis B surface antigen

1976 ◽  
Vol 3 (6) ◽  
pp. 626-631
Author(s):  
J Vnek ◽  
A M Prince
Keyword(s):  
Polyethylene Glycol ◽  
Hepatitis B ◽  
Surface Antigen ◽  
Phosphate Buffer ◽  
Sodium Phosphate ◽  
Large Scale ◽  
Hepatitis B Surface Antigen ◽  
Sodium Phosphate Buffer ◽  
Subsequent Elution ◽  
Polyethylene Glycol Precipitation

Hepatitis B surface antigen was concentrated and purified from plasma by two simple steps of purification. In the first step the antigen was purified 24-fold by polyethylene glycol precipitation. An additional 10-fold purification was achieved by batchwise adsorption to hydroxylapatite and subsequent elution with 0.02 M sodium phosphate buffer.

Sodium phosphate buffer (0.2 M)

2010 ◽  
Vol 2010 (1) ◽  
pp. pdb.rec12105-pdb.rec12105
Keyword(s):  
Phosphate Buffer ◽  
Sodium Phosphate ◽  
Sodium Phosphate Buffer

Association of glycerylphosphorylcholine with human sperm and effect of capacitation on their metabolism

1994 ◽  
Vol 6 (6) ◽  
pp. 679 ◽  
Author(s):  
J Mitra ◽  
M Chowdhury
Keyword(s):  
Oxidative Phosphorylation ◽  
Phosphate Buffer ◽  
Sodium Phosphate ◽  
Human Sperm ◽  
Cervical Mucus ◽  
Breakdown Product ◽  
O2 Uptake ◽  
Head Region ◽  
Aerobic Conditions ◽  
Sodium Phosphate Buffer

The presence and localization of glycerylphosphorylcholine (GPC) on the surface of human sperm, as well as the metabolism of its breakdown product L-glycerol 3 phosphate (G3P), were investigated. GPC was found to be associated with sperm after penetrating cervical mucus and was present after repeated washing of the sperm. GPC was partially released by treatment with 0.4 M NaCl in 0.01 M sodium phosphate buffer (pH 7.4) and localized to the head region after sperm fractionation. G3P did not increase O2 uptake of uncapacitated human sperm. However, under aerobic conditions, lactate accumulated when exogenous G3P or uterine GPC diesterase was added to sperm in suspension. The uptake of O2 by washed capacitated sperm pre-incubated with 1 unit of rat uterine GPC diesterase for 30 min was significant. This effect was inhibited by 2 microM oligomycin indicating that oxidative phosphorylation had occurred. The present study indicates that GPC may play a role in the metabolism of human sperm after capacitation.

scholarly journals Precise Method for the Measurement of Catalase Activity in Honey

2005 ◽  
Vol 88 (3) ◽  
pp. 800-804 ◽  
Author(s):  
José F Huidobro ◽  
M Pilar Sánchez ◽  
Soledad Muniategui ◽  
M Teresa Sancho
Keyword(s):  
Catalase Activity ◽  
Phosphate Buffer ◽  
Sodium Phosphate ◽  
Sample Volume ◽  
Dialysis Fluid ◽  
Sodium Phosphate Buffer ◽  
Relative Standard ◽  
Dialysis Membranes ◽  
Hcl Concentration

Abstract An improved method is reported for the determination of catalase activity in honey. We tested different dialysis membranes, dialysis fluid compositions and amounts, dialysis temperatures, sample amounts, and dialysis times. The best results were obtained by dialysis of 7.50 g sample in a cellulose dialysis sack, using two 3 L portions of 0.015M sodium phosphate buffer (pH 7.0) as the dialysis fluid at 4°C for 22 h. As in previous methods, catalase activity was determined on the basis of the rate of disappearance of the substrate, H2O2, with the H2O2 determined spectrophotometrically at 400 nm in an assay system containing o-dianisidine and peroxidase. Trials indicated that the best solvent for the o-dianisidine was 0.2M sodium phosphate buffer, pH 6.1; the best starting H2O2 concentration was 3mM; the best HCl concentration for stopping the reaction was 6N; and the best sample volume for catalase measurement was 7.0 mL. Precision values (relative standard deviations for analyses of 10 subsamples of each of 3 samples) were high, ranging from 0.48% for samples with high catalase activity to 1.98% for samples with low catalase activity.

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